Y5020_ARATH
ID Y5020_ARATH Reviewed; 1048 AA.
AC Q0WR59; Q8VYQ5; Q9LEA2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable inactive receptor kinase At5g10020;
DE Flags: Precursor;
GN OrderedLocusNames=At5g10020; ORFNames=T31P16.10, T31P16_9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- INTERACTION:
CC Q0WR59; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-16945916, EBI-20651541;
CC Q0WR59; C0LGL4: At2g28960; NbExp=2; IntAct=EBI-16945916, EBI-16946048;
CC Q0WR59; Q9XIC7: SERK2; NbExp=3; IntAct=EBI-16945916, EBI-6299033;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0WR59-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0WR59-2; Sequence=VSP_034563;
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; AL356332; CAB92043.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91482.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91483.1; -; Genomic_DNA.
DR EMBL; AY070134; AAL47484.1; -; mRNA.
DR EMBL; AK228463; BAF00390.1; -; mRNA.
DR PIR; T50006; T50006.
DR RefSeq; NP_001078562.1; NM_001085093.2. [Q0WR59-2]
DR RefSeq; NP_196564.1; NM_121040.4. [Q0WR59-1]
DR AlphaFoldDB; Q0WR59; -.
DR SMR; Q0WR59; -.
DR BioGRID; 16143; 29.
DR IntAct; Q0WR59; 32.
DR STRING; 3702.AT5G10020.1; -.
DR iPTMnet; Q0WR59; -.
DR PaxDb; Q0WR59; -.
DR PRIDE; Q0WR59; -.
DR ProteomicsDB; 243042; -. [Q0WR59-1]
DR EnsemblPlants; AT5G10020.1; AT5G10020.1; AT5G10020. [Q0WR59-1]
DR EnsemblPlants; AT5G10020.2; AT5G10020.2; AT5G10020. [Q0WR59-2]
DR GeneID; 830865; -.
DR Gramene; AT5G10020.1; AT5G10020.1; AT5G10020. [Q0WR59-1]
DR Gramene; AT5G10020.2; AT5G10020.2; AT5G10020. [Q0WR59-2]
DR KEGG; ath:AT5G10020; -.
DR Araport; AT5G10020; -.
DR TAIR; locus:2184058; AT5G10020.
DR eggNOG; ENOG502QWF1; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q0WR59; -.
DR OMA; RVMDCID; -.
DR PhylomeDB; Q0WR59; -.
DR PRO; PR:Q0WR59; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q0WR59; baseline and differential.
DR Genevisible; Q0WR59; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1048
FT /note="Probable inactive receptor kinase At5g10020"
FT /id="PRO_0000343175"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 100..120
FT /note="LRR 1"
FT REPEAT 124..146
FT /note="LRR 2"
FT REPEAT 148..169
FT /note="LRR 3"
FT REPEAT 172..194
FT /note="LRR 4"
FT REPEAT 196..217
FT /note="LRR 5"
FT REPEAT 224..246
FT /note="LRR 6"
FT REPEAT 250..272
FT /note="LRR 7"
FT REPEAT 273..294
FT /note="LRR 8"
FT REPEAT 298..319
FT /note="LRR 9"
FT REPEAT 320..342
FT /note="LRR 10"
FT REPEAT 365..387
FT /note="LRR 11"
FT REPEAT 389..411
FT /note="LRR 12"
FT REPEAT 412..433
FT /note="LRR 13"
FT REPEAT 436..457
FT /note="LRR 14"
FT REPEAT 469..491
FT /note="LRR 15"
FT REPEAT 493..516
FT /note="LRR 16"
FT REPEAT 517..539
FT /note="LRR 17"
FT REPEAT 540..560
FT /note="LRR 18"
FT DOMAIN 768..1045
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 696..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 774..782
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 796
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17586839,
FT ECO:0007744|PubMed:18433157"
FT VAR_SEQ 264..311
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_034563"
FT CONFLICT 720..724
FT /note="SSSGG -> CCSED (in Ref. 3; AAL47484)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="P -> H (in Ref. 3; AAL47484)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1048 AA; 114714 MW; 978E541CC6593390 CRC64;
MSHFLTFCFL SLLLLLHGAN AVTETELRSL LEFRKGIRDE TSHQRISWSD TSSLTDPSTC
PNDWPGISCD PETGSIIAIN LDRRGLSGEL KFSTLSGLTR LRNLSLSGNS FSGRVVPSLG
GISSLQHLDL SDNGFYGPIP GRISELWSLN HLNLSSNKFE GGFPSGFRNL QQLRSLDLHK
NEIWGDVGEI FTELKNVEFV DLSCNRFNGG LSLPMENISS ISNTLRHLNL SHNALNGKFF
SEESIGSFKN LEIVDLENNQ INGELPHFGS QPSLRILKLA RNELFGLVPQ ELLQSSIPLL
ELDLSRNGFT GSISEINSST LTMLNLSSNG LSGDLPSSFK SCSVIDLSGN TFSGDVSVVQ
KWEATPDVLD LSSNNLSGSL PNFTSAFSRL SVLSIRNNSV SGSLPSLWGD SQFSVIDLSS
NKFSGFIPVS FFTFASLRSL NLSRNNLEGP IPFRGSRASE LLVLNSYPQM ELLDLSTNSL
TGMLPGDIGT MEKIKVLNLA NNKLSGELPS DLNKLSGLLF LDLSNNTFKG QIPNKLPSQM
VGFNVSYNDL SGIIPEDLRS YPPSSFYPGN SKLSLPGRIP ADSSGDLSLP GKKHHSKLSI
RIAIIVASVG AAIMILFVLF AYHRTQLKDF HGRNRFTDQA TTRDTKFGRS SRPSLFNFSS
NVEQQSSSLS FSNDHLLTAN SRSLSGIPGC EAEISEQGAP ATSAPTNLLD DYPAASGRKS
SSGGSPLSSS PRFSDQPVML DVYSPDRLAG ELFFLDVSLK LTAEELSRAP AEVLGRSSHG
TLYKATLDNG HMLTVKWLRV GLVRHKKDFA REAKKIGSLK HPNIVPLRAY YWGPREQERL
LLSDYLRGES LAMHLYETTP RRYSPMSFSQ RLKVAVEVAQ CLLYLHDRAM PHGNLKPTNI
ILSSPDNTVR ITDYCVHRLM TPSGVAEQIL NMSALGYSAP ELSSASKPIP TLKSDVYAFG
VILMELLTRR SAGDIISGQT GAVDLTDWVR LCDQEGRRMD CIDRDIAGGE EFSKGMEDAL
AVAIRCILSV NERPNIRQVL DHLTSISA
